The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica).
The complete amino acid sequence of a major trypsin inhibitor (FMTI-II) from seeds of foxtail millet (Setaria italica) was determined by analysis of peptides derived from the reduced and S-carboxymethylated protein by digestion with TPCK-trypsin and Staphylococcus aureus V8 protease. FMTI-II consists of 67 amino acid residues, including 10 half-cystine residues which are involved in 5 disulfide bridges in the molecule. The established sequence had a high degree of homology to Bowman-Birk type inhibitors from leguminous and gramineous plants. The trypsin reactive-site peptide bond in FMTI-II also appears to be Lys (16)-Ser (17) by comparison with these sequences.
Tashiro
M
M
Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University.
Asao
T
T
Hirata
C
C
Takahashi
K
K
Kanamori
M
M
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry*; D006109:Poaceae; D012639:Seeds / Q000032:analysis* / Q000187:drug effects; D012697:Serine Endopeptidases / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
C067589:FMTI-II protein, Setaria italica; D010940:Plant Proteins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin